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Structure and function of plant aspartic proteinases [PDF]
FEBS Journal, 2004 Aspartic proteinases of the A1 family are widely distributed among plant species and have been purified from a variety of tissues. They are most active at acidic pH, are specifically inhibited by pepstatin A and contain two aspartic residues ...
Isaura Simões, CARLOS Faro
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Resuscitation, 1986
The nomenclature of proteinases and their role in shock are reviewed. The regulation of the kallikrein-kinin system, coagulation and fibrinolysis is described with special emphasis on the role of granulocytes for the proteolysis in shock particularly in the lung. The effect of proteinase inhibitors on such systems is described, together with proteinase
G, Schlag, H, Redl
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The nomenclature of proteinases and their role in shock are reviewed. The regulation of the kallikrein-kinin system, coagulation and fibrinolysis is described with special emphasis on the role of granulocytes for the proteolysis in shock particularly in the lung. The effect of proteinase inhibitors on such systems is described, together with proteinase
G, Schlag, H, Redl
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Acta Histochemica, 1987
A characteristic of lysosomal cysteine proteinases is given by their kinetic constants with specific substrates, their sequence homology, and their reactivity with monospecific polyclonal antibodies.
H, Kirschke, B, Wiederanders
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A characteristic of lysosomal cysteine proteinases is given by their kinetic constants with specific substrates, their sequence homology, and their reactivity with monospecific polyclonal antibodies.
H, Kirschke, B, Wiederanders
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Natural protein proteinase inhibitors and their interaction with proteinases
European Journal of Biochemistry, 1992The substrate‐like ‘canonical' inhibition by the ‘small’ serine proteinase inhibitors and the product‐like inhibition by the carboxypeptidase inhibitor have provided the only atomic models of protein inhibitor–proteinase interactions for about 15 years.
W, Bode, R, Huber
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Proteinases and Proteinase Inhibitors
1992The peritoneal cavity is well endowed with proteinases both in the parietal and viseral peritoneum as well as in the peritoneal fluid. Proteinases have a major role in activating and modulating the complement, coagulation, kinin, fibrinolytic, and extracellular matrix remodeling systems, and thus are critical components of the peritoneal response to ...
Gere S. diZerega, Kathleen E. Rodgers
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Proteinase and Proteinase Inhibitor Localization in the Human Placenta
International Journal of Gynecological Pathology, 1989Standard immunoperoxidase techniques were used to investigate the distribution of the intracellular proteinase cathepsin D, two serine proteinase inhibitors--alpha 1-antitrypsin (alpha 1-AT) and alpha 1-antichymotrypsin (alpha 1-AChy)--and plasma fibrin stabilizing factor XIII (FXIII) in paraffin-embedded tissues from early and late intrauterine ...
U, Earl +3 more
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Acrosomal Proteinase and Proteinase Inhibitor of Human Spermatozoa
Science, 1972The acrosomal proteinase of human spermatozoa was characterized and differs from other human proteinases. The enzyme has optimal activity at p H 8.0, is inactive below p H 5.0 or above p H 10.5, requires calcium for maximum activity, hydrolyzes fibrinogen, gelatin, and
L J, Zaneveld +2 more
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Collagenolytic proteinases in keratoconus
American Journal of Ophthalmology, 2006To study the proteolytic phenomena contributing to the pathogenesis of keratoconus, corneal enzymes with potential to cleave fibrillar collagen were studied.Immunohistochemical labeling was undertaken of conventional and novel mammalian collagenases (MMP-1, -2, -8, -13, and -14) of the matrix metalloproteinase (MMP) family and other collagenolytic ...
Zygmunt, Mackiewicz +5 more
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British Medical Bulletin, 1995
The primary agents responsible for cartilage and bone destruction in joint diseases are active proteinases degrading collagen and proteoglycan. All four main classes of proteolytic enzymes are involved in either the normal turnover of connective tissue or its pathological destruction.
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The primary agents responsible for cartilage and bone destruction in joint diseases are active proteinases degrading collagen and proteoglycan. All four main classes of proteolytic enzymes are involved in either the normal turnover of connective tissue or its pathological destruction.
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Journal of Histochemistry & Cytochemistry, 1981
Our interest in proteolytic enzymes derives from our work on the pathogenesis of multiple sclerosis (MS). In this disease of the central nervous system the myelin sheaths enveloping the axons disintegrate, usually in a patchy manner beginning around small veins or near the ventricles, resulting in lesions or “plaques.” The cause of MS is still unknown.
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Our interest in proteolytic enzymes derives from our work on the pathogenesis of multiple sclerosis (MS). In this disease of the central nervous system the myelin sheaths enveloping the axons disintegrate, usually in a patchy manner beginning around small veins or near the ventricles, resulting in lesions or “plaques.” The cause of MS is still unknown.
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